ID R7YMW9_CONA1 Unreviewed; 785 AA.
AC R7YMW9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE RecName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_02366 {ECO:0000313|EMBL:EON63139.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63139.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; JH767561; EON63139.1; -; Genomic_DNA.
DR RefSeq; XP_007778456.1; XM_007780266.1.
DR AlphaFoldDB; R7YMW9; -.
DR STRING; 1168221.R7YMW9; -.
DR GeneID; 19899677; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR OMA; RDIRYET; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000016924}.
FT DOMAIN 22..483
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 143..343
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 714..785
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 785 AA; 86954 MW; 32D408BC503339BC CRC64;
MAIEKLPQRI FDQIQDDAGR PLIKRLLIAN RGEIACRVVA TCRKLNITSI AVYTDPDTHS
LHVQEADEAV RLGAIDGPEG NPHQNIQLLI QTALAHNADA IHPGYGYLSE NAEFSRQVRE
AGIIFLGPSP NSMAILGDKR SAKQYLLKNA PKIPLIPGYN GTEQTVDRLL IEADRIGFPI
LIKASAGGGG KGMRIVRHRE QLRDELNRAQ SEAQRSFGSS DCILERYIQR SKHIEIQILG
DNHGTIVSLM DRECSIQRRH QKIIEEAPSP WLKPALRQKM SETAVAIGKL LDYESAGTVE
FIVDVETTEF FFLEVNTRIQ VEHPITEETT GVDIVGLQIF VAGGGHLDDL GYWHDGMAPQ
VGHAIECRLC AEDPSRDFMP DLGFLRQWKT ASEILPSAQT QDVRFETGIA TGSQVSIYFD
SLIAKIVVWA PTRRQAIEKM VKMLAYTVCI GIRSNQSFLQ SCLLHPKFRD PEYSTSFIPD
LLPTLIKNPY VDDLLATQGK LSFLPSILRR QASLPSVQNN RQSFRSLPRS FRNQKADLAN
AQADVVLVPA HPEKIFIVAW PSSRSPEKFH NVTILPLSKQ DIQKSTEKVS SEDVKPSIQL
ALDYNQVSSH VRQLPRPGQT SSLSHEVSLS IRATSVFQQT PDSTWHLHEL FVSVDTQRYT
VFAVSAASSP GTDVGSHQKF FAHIPALGTY IEYNLCSLLT YGESLRKDTG ESAVASQRSP
KAPMPCKVLN VAKKDGETVK VGEIAVVVES MKMEMNILAA AEGIFRAKVA MGEAVEEGTV
LFTIS
//